期刊
EMBO JOURNAL
卷 25, 期 9, 页码 1816-1826出版社
WILEY
DOI: 10.1038/sj.emboj.7601078
关键词
actin; annexin; calcium; capping protein; cytoskeleton
资金
- MRC [G0100200] Funding Source: UKRI
- Medical Research Council [G0100200] Funding Source: researchfish
- Medical Research Council [G0100200] Funding Source: Medline
Annexin 2 is a ubiquitous Ca2+-binding protein that is essential for actin-dependent vesicle transport. Here, we show that in spontaneously motile cells annexin 2 is concentrated in dynamic actin-rich protrusions, and that depletion of annexin 2 using siRNA leads to the accumulation of stress fibres and loss of protrusive and retractile activity. Cells co-expressing annexin 2-CFP and actin-YFP exhibit Ca2+-dependent fluorescense resonance energy transfer throughout the cytoplasm and in membrane ruffles and protrusions, suggesting that annexin 2 may directly interact with actin. This notion was supported by biochemical studies, in which we show that annexin 2 reduces the polymerisation rate of actin monomers in a dose-dependent manner. By measuring actin polymerisation rates in the presence of barbed-end and pointed-end cappers, we further demonstrate that annexin 2 specifically inhibits filament elongation at the barbed ends. These results show that annexin 2 has an essential role in maintaining the plasticity of the dynamic membrane-associated actin cytoskeleton, and that its activity in this context may be at least partly explained through direct interactions with polymerised and monomeric actin.
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